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Sally L. Gras
Researcher at University of Melbourne
Publications - 162
Citations - 5210
Sally L. Gras is an academic researcher from University of Melbourne. The author has contributed to research in topics: Amyloid & Fibril. The author has an hindex of 31, co-authored 155 publications receiving 4220 citations. Previous affiliations of Sally L. Gras include University of Adelaide & Leiden University.
Papers
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Journal ArticleDOI
Metastability of native proteins and the phenomenon of amyloid formation.
Andrew Baldwin,Tuomas P. J. Knowles,Gian Gaetano Tartaglia,Anthony W. P. Fitzpatrick,Glyn L. Devlin,Sarah L. Shammas,Christopher A. Waudby,Maria F. Mossuto,Sarah Meehan,Sally L. Gras,John Christodoulou,Spencer J. Anthony-Cahill,Paul D. Barker,Michele Vendruscolo,Christopher M. Dobson +14 more
TL;DR: An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils reveals that this structural form is likely to be the most stable one that protein molecules can adopt even under physiological conditions, challenging the conventional assumption that functional forms of proteins correspond to the global minima in their free energy surfaces.
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Two-Dimensional Transition Metal Dichalcogenides in Biosystems
Kourosh Kalantar-zadeh,Jian Zhen Ou,Torben Daeneke,Michael S. Strano,Martin Pumera,Sally L. Gras +5 more
TL;DR: The intriguing properties of two-dimensional transition metal dichalcogenides (2D TMDCs) have led to a significant body of fundamental research and rapid uptake of these materials in many applications as mentioned in this paper.
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Recent advances refining galactooligosaccharide production from lactose
TL;DR: This review covers the broad but related aspects of GOS synthesis including: the structure and reaction mechanism of β-galactosidase, factors effecting yield and productivity ofGOS synthesis systems, the structure of G OS products, models for the kinetics of Gos synthesis and reactor configurations for GOS synthesisation.
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Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alpha(s-) and beta-casein
David C. Thorn,Sarah Meehan,Margaret Sunde,Agata Rekas,Sally L. Gras,Cait E. MacPhee,Christopher M. Dobson,Mark R Wilson,John A. Carver +8 more
TL;DR: It is suggested that alphaS- and beta- casein are potent inhibitors of kappa-casein fibril formation and may prevent large-scale fibrils formation in vivo and play a preventative role in the development of corpora amylacea, a disorder associated with the accumulation of amyloid deposits in mammary tissue.
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Functionalised amyloid fibrils for roles in cell adhesion
Sally L. Gras,Anna K Tickler,Adam M. Squires,Glyn L. Devlin,Michael A. Horton,Christopher M. Dobson,Cait E. MacPhee +6 more
TL;DR: It is suggested that it will be possible to generate nanomaterials based on amyloid fibrils that are tailored to promote interactions with a wide variety of cell types.